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Database: UniProt
Entry: A4SRI4_AERS4
LinkDB: A4SRI4_AERS4
Original site: A4SRI4_AERS4 
ID   A4SRI4_AERS4            Unreviewed;       392 AA.
AC   A4SRI4;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Peptidase A2 domain-containing protein {ECO:0000259|PROSITE:PS50175};
GN   OrderedLocusNames=ASA_3538 {ECO:0000313|EMBL:ABO91506.1};
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO91506.1, ECO:0000313|Proteomes:UP000000225};
RN   [1] {ECO:0000313|Proteomes:UP000000225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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DR   EMBL; CP000644; ABO91506.1; -; Genomic_DNA.
DR   RefSeq; WP_005318740.1; NC_009348.1.
DR   AlphaFoldDB; A4SRI4; -.
DR   KEGG; asa:ASA_3538; -.
DR   PATRIC; fig|382245.13.peg.3521; -.
DR   eggNOG; ENOG502Z9XK; Bacteria.
DR   HOGENOM; CLU_057078_0_0_6; -.
DR   Proteomes; UP000000225; Chromosome.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05483; retropepsin_like_bacteria; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR034122; Retropepsin-like_bacterial.
DR   Pfam; PF13650; Asp_protease_2; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..392
FT                   /note="Peptidase A2 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002673503"
FT   DOMAIN          56..71
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
SQ   SEQUENCE   392 AA;  42992 MW;  CA1416D3E312805B CRC64;
     MTLQFNAMAL AILILSAVQG CSVPDSSATA TPSAPVLAVH YESAPLIPVT IAGEQYQFLL
     DTGASITVID RRLASRFKAL SLSELPRAYQ ADFANVASVS GQVGSDQLGF VQPVPFSVGS
     VTIDDSDLWG TMDFELFSQS IGTRIDGVLG IDTIRRFNWV FDNEQHQISA SLRVPSAAAF
     ERCIGYEDSY NRSPAIYLTH GESSVRMYLD TGADQSYVDR AFIDFMADKQ ALLGAGASPR
     KGADASGMQA ASEHILTDLQ FDERPLGQLR VSENGNDKYA LGLDFVNRFK RFAIIPGRMM
     ICYDAGSLAR QLPPFLRNIA VRFDGQHLQI YYNDEQALTP YGLKNGDLIE RVNGVAYRPI
     EIDKVRELLN ISKPGSLKMR VIREGKALDI AI
//
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